A0A9W8DXN8 · A0A9W8DXN8_9FUNG
- ProteinArginine biosynthesis bifunctional protein ArgJ, mitochondrial
- GeneECM42
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids601 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of acetylglutamate from glutamate and acetyl-CoA, and of ornithine by transacetylation between acetylornithine and glutamate.
Catalytic activity
- L-glutamate + N2-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate
Pathway
Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N2-acetyl-L-ornithine (cyclic): step 1/1.
Amino-acid biosynthesis; L-arginine biosynthesis; N2-acetyl-L-ornithine from L-glutamate: step 1/4.
Features
Showing features for site, binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 295 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | ||||
Sequence: T | ||||||
Site | 296 | Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole | ||||
Sequence: G | ||||||
Binding site | 332 | substrate | ||||
Sequence: T | ||||||
Binding site | 362 | substrate | ||||
Sequence: K | ||||||
Site | 372-373 | Cleavage; by autolysis | ||||
Sequence: AT | ||||||
Active site | 373 | Nucleophile | ||||
Sequence: T | ||||||
Binding site | 373 | substrate | ||||
Sequence: T | ||||||
Binding site | 468 | substrate | ||||
Sequence: E | ||||||
Binding site | 596 | substrate | ||||
Sequence: N | ||||||
Binding site | 601 | substrate | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Molecular Function | acetyl-CoA:L-glutamate N-acetyltransferase activity | |
Molecular Function | glutamate N-acetyltransferase activity | |
Biological Process | arginine biosynthetic process | |
Biological Process | ornithine biosynthetic process |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameArginine biosynthesis bifunctional protein ArgJ, mitochondrial
- Cleaved into 2 chains
Including 2 domains:
- Recommended nameGlutamate N-acetyltransferase
- EC number
- Short namesGAT
- Alternative names
- Recommended nameAmino-acid acetyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Fungi incertae sedis > Zoopagomycota > Kickxellomycotina > Kickxellomycetes > Kickxellales > Kickxellaceae > Mycoemilia
Accessions
- Primary accessionA0A9W8DXN8
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-17 | |||||
Sequence: MKAAFFSTIAIAAVAYA | ||||||
Chain | PRO_5041027312 | 1-372 | Arginine biosynthesis bifunctional protein ArgJ alpha chain | |||
Sequence: MKAAFFSTIAIAAVAYAADSSSESASDSAVPSVSVPEISSFSWSDSPQAKCVKDNCGDANDLSCVAQCYGVPNPNSQMINDTDGCFKKCEGISGAEQCRAACIDQFYNPTTGEFARPTASDDSSASGKSGSKEHKSGDKNKSNSDGESDSEGSATKFTASLGAAFPEKKIKFIPTSGTYPKGFLAGGSHCGVKKNSAPDLAMLFSQKPCTAAAVFTKNQFCAAPVQFDRSLLNKIAESGQQKIRCAVINSGCANAVTGTEGLENASRMANAANQFVSKHDGGSENVSCASLIMSTGVIGQQLPIGKIENGIKDLKLDSTHEAWMRAAIAHMTTDTFPKLRSVEYTLEDGDSATKYRFAGITKGAGMIHPNMA | ||||||
Chain | PRO_5040896093 | 18-601 | Arginine biosynthesis bifunctional protein ArgJ, mitochondrial | |||
Sequence: ADSSSESASDSAVPSVSVPEISSFSWSDSPQAKCVKDNCGDANDLSCVAQCYGVPNPNSQMINDTDGCFKKCEGISGAEQCRAACIDQFYNPTTGEFARPTASDDSSASGKSGSKEHKSGDKNKSNSDGESDSEGSATKFTASLGAAFPEKKIKFIPTSGTYPKGFLAGGSHCGVKKNSAPDLAMLFSQKPCTAAAVFTKNQFCAAPVQFDRSLLNKIAESGQQKIRCAVINSGCANAVTGTEGLENASRMANAANQFVSKHDGGSENVSCASLIMSTGVIGQQLPIGKIENGIKDLKLDSTHEAWMRAAIAHMTTDTFPKLRSVEYTLEDGDSATKYRFAGITKGAGMIHPNMATLLGTICTDVSISQPLLAKALLHAVNRSFNSISIDGDTSTNDTISVLANGAADESYVANSGKYTISSENSEAYERFQTALTEFAVDLASLVVRDGEGATKFITIRVKGAKTYDEGKTIASTIATSALVKTAFYGQDANWGRILCAVGYSGVPVDTAKVNLSLIPSDGSKSLPLVISGEPLVVDEVRAKEILTLEDVSVEVDLGLGNETVQMYTCDFSHDYVSINADYRS | ||||||
Chain | PRO_5041027313 | 373-601 | Arginine biosynthesis bifunctional protein ArgJ beta chain | |||
Sequence: TLLGTICTDVSISQPLLAKALLHAVNRSFNSISIDGDTSTNDTISVLANGAADESYVANSGKYTISSENSEAYERFQTALTEFAVDLASLVVRDGEGATKFITIRVKGAKTYDEGKTIASTIATSALVKTAFYGQDANWGRILCAVGYSGVPVDTAKVNLSLIPSDGSKSLPLVISGEPLVVDEVRAKEILTLEDVSVEVDLGLGNETVQMYTCDFSHDYVSINADYRS |
Post-translational modification
The alpha and beta chains are autoproteolytically processed from a single precursor protein within the mitochondrion.
Keywords
- PTM
Interaction
Subunit
Heterodimer of an alpha and a beta chain.
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 113-154 | Disordered | ||||
Sequence: EFARPTASDDSSASGKSGSKEHKSGDKNKSNSDGESDSEGSA | ||||||
Compositional bias | 127-146 | Basic and acidic residues | ||||
Sequence: GKSGSKEHKSGDKNKSNSDG |
Sequence similarities
Belongs to the ArgJ family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length601
- Mass (Da)63,234
- Last updated2023-11-08 v1
- Checksum50F99E13BA491CF7
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 127-146 | Basic and acidic residues | ||||
Sequence: GKSGSKEHKSGDKNKSNSDG |
Keywords
- Technical term